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PubMed2004

Acidic proteome of growing and resting Lactococcus lactis metabolizing maltose.

The acidic proteome of Lactococcus lactis grown anaerobically was compared for three different growth conditions: cells growing on maltose, resting cells metabolizing maltose, and cells growing on glucose. In maltose metabolizing cells several proteins were up-regulated compared with glucose metabolizing cells, however only some of the up-regulated proteins had apparent relation to maltose metabolism. Cells growing on maltose produced formate, acetate and ethanol in addition to lactate, whereas resting cells metabolizing maltose and cells growing on glucose produced only lactate. Increased levels of alcohol-acetaldehyde dehydrogenase (ADH) and phosphate acetyltransferase (PTA) in maltose-growing cells compared with glucose-growing cells coincided with formation of mixed acids in maltose-growing cells. The resting cells did not grow due to lack of an amino acid source and fermented maltose with lactate as the sole product, although ADH and PTA were present at high levels. The maltose consumption rate was approximately three times lower in resting cells than in exponentially growing cells. However, the enzyme levels in resting and growing cells metabolizing maltose were similar, which indicates that the difference in product formation in this case is due to regulation at the enzyme level. The levels of 30S ribosomal proteins S1 and S2 increased with increasing growth rate for resting cells metabolizing maltose, maltose-growing cells and glucose-growing cells. A modified form of HPr was synthesized under amino acid starvation. This is suggested to be due to alanine misincorporation for valine, which L. lactis is auxotrophic for. L. lactis conserves the protein profile to a high extent, even after prolonged amino acid starvation, so that the protein expression profile of the bacterium remains almost invariant.

Acetates↗
PubMed1998

Archael phosphoproteins. Identification of a hexosephosphate mutase and the alpha-subunit of succinyl-CoA synthetase in the extreme acidothermophile Sulfolobus solfataricus.

When soluble extracts from the extreme acidophilic archaeon Sulfolobus solfataricus were incubated with [gamma-32P]ATP, several radiolabeled polypeptides were observed following SDS-PAGE. The most prominent of these migrated with apparent molecular masses of 14, 18, 35, 42, 46, 50, and 79 kDa. Phosphoamino acid analysis revealed that all of the proteins contained phosphoserine, with the exception of the 35-kDa one, whose protein-phosphate linkage proved labile to strong acid. The observed pattern of phosphorylation was influenced by the identity of the divalent metal ion cofactor used, Mg2+ versus Mn2+, and the choice of incubation temperature. The 35- and 50-kDa phosphoproteins were purified and their amino-terminal sequences determined. The former polypeptide's amino-terminal sequence closely matched a conserved portion of the alpha-subunit of succinyl-CoA synthetase, which forms an acid-labile phosphohistidyl enzyme intermediate during its catalytic cycle. This identification was confirmed by the ability of succinate or ADP to specifically remove the radiolabel. The 50-kDa polypeptide's sequence contained a heptapeptide motif, Phe/Pro-Gly-Thr-Asp/Ser-Gly-Val/Leu-Arg, found in a similar position in several hexosephosphate mutases. The catalytic mechanism of these mutases involves formation of a phosphoseryl enzyme intermediate. The identity of p50 as a hexosephosphate mutase was confirmed by (1) the ability of sugars and sugar phosphates to induce removal of the labeled phosphoryl group from the protein, and (2) the ability of [32P]glucose 6-phosphate to donate its phosphoryl group to the protein.

Adenosine Diphosphate↗
PubMed2001

Kinetic mechanism and pH dependence of the kinetic parameters of Pseudomonas aeruginosa phosphomannomutase/phosphoglucomutase.

The enzyme phosphomannomutase/phosphoglucomutase (PMM/PGM) is responsible for the formation of mannose 1-phosphate and glucose 1-phosphate in the human pathogenic bacterium Pseudomonas aeruginosa. Mannose 1-phosphate and glucose 1-phosphate are required for the biosynthesis of polysaccharides that contribute to the virulence of P. aeruginosa, so inhibitors of PMM/PGM may lead to clinically useful compounds. The V/K values for mannose 6-phosphate and glucose 6-phosphate show that they are equally good substrates for the enzyme. PMM/PGM overexpressed in Escherichia coli is isolated as a phosphoenzyme; surprisingly, mutation of serine 108 where phosphorylation occurs results in phosphorylation of a different residue so that activity is reduced only 20-fold from that of wild-type enzyme. In the reverse reaction glucose 1-phosphate exhibits substrate inhibition, which arises through its competition with the activator glucose 1,6-bisphosphate for binding to dephosphoenzyme. This phenomenon is consistent with a mechanism in which the enzyme phosphorylates the substrate to generate a bisphosphorylated intermediate that reorients in the active site to return its original phosphoryl group to the enzyme and generate the observed product. The pH dependence of the kinetic parameters suggests that the active site contains a residue that serves as a general base in the catalytic reaction and one that acts as a general acid. However, the pK of the general acid is 7.4 and that of the general base is 8.4 so these residues exist in a state of reverse protonation in the active enzyme.

Alginates↗
PubMed2002

Mutation in the Xanthomonas campestris xanA gene required for synthesis of xanthan and lipopolysaccharide drastically reduces the efficiency of bacteriophage (phi)L7 adsorption.

(Phi)L7 is a lytic phage infecting the gram-negative Xanthomonas campestis pv. campestris, a plant pathogen. To study phage-host interaction, a (phi)L7-resistant mutant was isolated from strain Xc17 by mini-Tn5 transposition and designated CH7LR. CH7LR could not plate (phi)L7 in double-layered assay and formed turbid clearing zones when the cell lawn was dropped with a high titer of (phi)L7. Sequence analysis showed that the mutated gene is xanA coding for phosphoglucomutase/phosphomannomutase, required for the synthesis of lipopolysaccharide and exopolysaccharide (xanthan). The involvement of xanA was confirmed by isolating another mutant with interrupted xanA and complementing with the cloned wild-type gene. Nonmucoid mutants are still sensitive to (phi)L7, indicating that xanthan is not involved in (phi)L7 adsorption. Since the mutants still exhibited low efficiencies of phage adsorption, we predict, by analogy with the cases in other bacteriophages of gram-negative bacteria, that other outer membrane components such as a protein are required for the formation of a complex receptor.

Adsorption↗
PubMed1995

Exploratory analysis of population genetic assessment as a water quality indicator. I. Pimephales notatus.

Biological sampling has been implemented to assess water quality in many states. The purpose of this study was to examine whether genetic diversity and structure of Pimephales notatus could serve as effective biomarkers of exposure to anthropogenic stressors by comparing genetic measures with other biological indicators of water quality. Fish were collected from 15 sites on eight streams by the Ohio Environmental Protection Agency as part of their stream water quality evaluation program. Values for the Index of Biotic Integrity (IBI) and the Invertebrate Community Index (ICI) were determined for these 15 sites. Starch gel electrophoresis was used to collect genetic data for seven variable enzyme loci. Genetic diversity measures were not associated with site IBI or ICI values. However, the range of site IBI and ICI values was limited. The proportion of individuals not expressing esterase locus 3 could be used to predict IBI; IBI decreased as the proportion of nonexpression increased. Allele and genotype frequency differences were observed between sites on the Little Scioto River, the one stream with a large difference in IBI and ICI values between sites. This study suggested that allele and genotype frequencies may have been impacted without affecting overall species diversity.

Alleles↗
PubMed1995

Exploratory analysis of population genetic assessment as a water quality indicator. II. Campostoma anomalum.

Biological monitoring programs to assess contaminant-induced impacts in aquatic systems are being developed and implemented by several federal agencies and many states. Genetic diversity and allozyme frequency may be valuable indicators of such impact because they are both sensitive to exposure and ecologically relevant in populations. The purpose of this study was to examine whether genetic diversity and structure of Campostoma anomalum populations could serve as effective biomarkers of exposure to anthropogenic stress by comparing genetic measures with other biological indicators of water quality. Fish were collected from 14 sites on seven streams by the Ohio Environmental Protection Agency as part of their stream water quality evaluation program. Values for the Index of Biological Integrity (IBI) and the Invertebrate Community Index (ICI) were determined for these 14 sites. Starch gel electrophoresis was used to collect genetic data for eight variable enzyme loci. Genetic diversity measures were not associated with site IBI or ICI values. However, the range of site IBI and ICI values was limited. Allele and genotype frequencies were significantly different at the point source compared to sites upstream and downstream indicating that genetic structure may be an indicator of water quality that is sensitive enough to detect change prior to species loss.

Acid Phosphatase↗
PubMed1981

[Influence of aging of blood samples and traces on the pattern of PGM1- and Gc-subtypes (author's transl)].

The isozymes of the PGMa1-system can be determined more or less distinctly in stored blood samples up to 1.5 years in approximately half of all samples. However, in several cases shifting of the isoelectric points and splitting can be noticed, especially in the c-bands range and, as a result of this, the primary type PGM1 a1 can simulate a PGM1 a2-a1 type, or more rarely a PGM1 a2 type. By a small cathodic shift of the a-band even PGM1 a3-a2 type can be found under special circumstances. Dried traces may simulate the PGM1 a2-a1 type through the appearance of conversion-bands in the b-range and on definite trace carriers even the PGM1 a4-a1 type may be simulated. The presentation of the Gc-subtypes is nearly always possible parallel to the Tf-subtypes even in alcohol blood samples stored for up to 3 months and in most of those stored for up to 7 months. Later, it often comes to a widening and splitting of the 1-band so that a discrimination of the S- and F-homo- and heterozygotes, respectively, is not possible anymore. Altogether, Gc-basic types may be more easily determined by isoelectric focusing in aged blood samples than with the electrophoretic methods including immunofixation.

Blood Stains↗
PubMed1984

[Rare PGM1 (6) and PGM1(7) alleles in the Polish population].

Rare PGM1 phenotypes, 6-1, 6-2 and 7-2, were detected in blood samples from 3,437 non-related adults using electrophoresis in starch-gel and cellulose acetate membranes. Frequencies of 0.0009 and 0.0008 were calculated for PGM1(6) and PGM1(7), respectively, for a population from northern Poland. The variants had been inherited, which was confirmed by family studies.

Adult↗
PubMed1977

Characterization of a regulatory mutant of fructose 1,6-bisphosphatase in Saccharomyces carlsbergensis.

The fdp mutation has been localized on the genome of Saccharomyces carlsbergensis, on chromosome II, between lys2 and tyr1, at a man distance of 31 centimorgan from lys2. Since the fdp mutant does not grow on glucose, fructose, mannose and sucrose, hexose transport and a number of enzymes of carbon metabolism were tested, but no significant differences could be found between the wild type and the mutant. Only the regulatory properties of glycogen synthetase are changed in the mutant, but it is doubtful whether this can explain its phenotype. The disorganization of carbon metabolism of the mutant upon addition of glucose to the medium was analyzed in more detail. The most prominent feature observed until now is the accumulation of free glucose and hexose phosphates in the cell. This result indicates that somehow the feedback control between hexose transport and metabolism is impaired. Hexose phosphates are known to be toxic to many cells, including yeast. Therefore, accumulation of hexose phosphates in the presence of glucose in the medium, can explain the absence of growth on this carbon source.

Alcohol Oxidoreductases↗
PubMed1985

Gene localisation of the PGM1 enzyme system and the Duffy blood groups on chromosome No. 1 by means of a new fragile site at 1p31.

During routine paternity testing an apparent maternal exclusion was suggested by the PGM1 enzyme system (mother PGM1 1, child PGM1 2) and by the Duffy system (mother Fy(a-b+), child Fy(a+b-]. To clarify these findings chromosomal analyses and anthropological investigations were carried out. The possibility that the child had been mistakenly identified after birth could be eliminated. Chromosome analysis of the child showed a fragile site on one chromosome No. 1 at 1p31, a position supposed to carry the PGM1 and the Duffy loci. Although the father of the child is unknown, paternal origin of the fragile site is unlikely on account of the coincidence of the structural aberration with the missing expression of the maternal PGM1 and Duffy alleles thought to be located at the chromosome region involved. Thus localisation of the PGM1 and Duffy loci on 1p31 seems to have been achieved in an unusual way. The two loci appear to be closely linked.

Alleles↗
PubMed1975

On the distribution of some genetic markers in libya.

On a sample of N equals 169 nonrelated blood donors from Libya several blood group, serum protein group and enzyme frequencies are within the range of those of other Caucasoid populations. However, the frequencies of cDe, Jk-a, Fy-c, Hp-1, Gc-1, aP-b and AK-1 show some greater differences and seem to indicate certain Negroid influence on the genetic composition of our Libyan sample. This assumption is conceivable considering the racial history of Libya.

Acid Phosphatase↗